Aquaporin-7 Antibodies

Aquaporin-7 (AQP7)

Forms a channel for water and glycerol. .

Gene Information

Human
Gene Name:	AQP7
Uniprot:	O14520
Entrez:	364

Family

Belongs to:
MIP/aquaporin (TC 1.A.8) family

Alternative Names

AQP-7; AQP7L; AQP9MGC149556; AQPapaquaglyceroporin-7; Aquaglyceroporin-7; aquaporin 7; Aquaporin adipose; aquaporin-7; Aquaporin-7-like; MGC149555

Molecular Weight

Mass (kDA):
37.232 kDA

Genomic Context

Human
Location:	9p13.3
Sequence:	9; NC_000009.12 (33383135..33402682, complement)

Subcellular Localizations

Cell membrane; Multi-pass membrane protein. Cytoplasm, cell cortex. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Lipid droplet. Internalized from the cell membrane in response to catecholamine-induced activation of PKA; detected on intracellular membranes and colocalizes with lipid droplets (By similarity). Colocalizes with PLIN1 in adipocytes, probably on lipid droplets (PubMed:27832861).

Diseases

• Obesity
• Diabetes Mellitus
• Edema
• Insulin Resistance
• Diabetes Mellitus, Non-insulin-dependent
• Nephrogenic Diabetes Insipidus
• Obesity, Morbid
• Ischemia
• Hyperglycemia
• Kidney Failure
• Kidney Diseases
• Disease Of Adrenal Medulla

• Malignant Neoplasms
• Neoplasms
• Impaired Glucose Tolerance
• Hypertrophy
• Endolymphatic Hydrops
• Male Infertility
• Insulin Sensitivity

Pathways

• Transport
• Localization
• Water Transport
• Secretion
• Glycerol Transport
• Gluconeogenesis
• Water Homeostasis
• Urea Transport
• Spermatogenesis
• Cell Migration
• Glucose Homeostasis
• Fluid Transport
• Cellular Localization

• Fertilization
• Cell Proliferation
• Insulin Secretion
• Secretory Pathway
• Methylation
• Sperm Motility
• Pathogenesis

PTMs

• Phosphorylation

• Glycosylation

• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/AQP7

Best Uses of the AQP7 Marker

How can you best use the AQP7 marker in your research? The AQP7Marker has many benefits and potential uses. Below are just a few. These biomarkers have many benefits for scientists all over the world. You can also learn about their variants and constructions. These methods can also be used to test a broad range of proteins.

AQP7 Signer

The AQP7 marker has been proven to be a useful tool in the study of sperm movement and morphology. It has been identified in motile and ejaculated sperm that swim up-and-down. AQP7 was immunolabeled in the mitochondrial portion of ejaculated sperm. Different techniques were used to study the distribution and mathematical elaboration of AQP7 inside sperm.

The AQP7 genes plays a function in regulation of lipolysis. They alter the glycerol channel located at the plasma membrane. The local glycerol content in adipocytes is reduced by AQP7, which influences the chemical composition of lipolysis. Additional research is required to identify the mediators responsible in the interaction of AQP7 with CGI-58 within adipocytes.

The cytoplasmic AQP monomer, which weighs 28-30 kDa, has a 28-30 kDa weight. It forms a barrel shape across the plasma membrane and has six ahelical domains. The monomer is composed of a single chain of 270 amino acids with amino terminals in the cytoplasm. The AQP is composed of two conserved sequence motifs known as NPA motifs. These motifs are bent into the molecule, and then pair to form a water channel. In addition to the cysteine residue, many AQPs are also found in extracellular orientations. This can block transport of AQPs that have a mercury-sensitive function.

Overexpression of the AQP7 marker has been found in several cancer types. It was found in breast cancer and colon cancers but not in invasive ductal carcinomas. Its increased expression is linked to other AQPs. The gene can also be found in different types of tumors including lung and colorectal. This gene can be used as a therapeutic target and diagnostic biomarker for brain cancer.

AQP1-Luc

Boster Bio has the AQP1 Luc Antibody, which is a high specificity, high-sensitivity anti-aquaporin antibody. This antibody was approved for use in IHC and Flow Cytometry. Boster Bio’s AQP1–Luc antibody reacts in the same way with Rat, Mouse, Human. It can also be used in ELISA.

The luciferase reporters constructed from the first 1kb of the mouse exon were designed for assessing the roles of TonEBP consensus sites. The luciferase activity in AQP1-Luc could be decreased or maintained by substituting a TTTCGACCTC site. This study supports the hypothesis that the TonEBP consensus site is involved in the transcription of the AQP1 promoter under hypertonic conditions.

AQP1 (a 28-kD integral proteins) is found in many tissues and organs. It was previously thought to be a Rh monopeptide breakdown product. It was later found to be a distinct molecule. The aquaporin channel is found in plasma membranes and allows water to flow in the direction of an organic gradient.

A circadian rhythmicity is also observed in the expression of core clock genes Bmal1-dLuc, and Per2-dLuc. These oscillations occur in mature cardiac tissues transduced by these lentiviral-plasmids. These oscillations are also found in older in vitro cultures. The study is therefore valuable in studying cardiac function.

The single-stranded DNA dependent ATPase activity is retained by the mutant PriA protein. However, the luciferase activity can be normalized to b -galactosidase. AQP1Luc transfection is a good option for the development of therapies. However, these transfections should only be used with the approval of clinical trials.

AQP4-Luc

The monoclonal AQP4-IgG recombinant antibody (AQP4-IgG) binds to a region on AQP4 that is consistent with cellular fluorescence. These antibodies are made specifically to detect M23-AQP4. The binding affinity AQP4IgGs varied from almost identical to exclusive. However, the tightest AQP4IgG showed an affinity that was only fifteen nanometers. This indicates that monoclonal AQP4–IgGs will be more likely to bind the AQP4–Luc proteins.

AQP4-4-Luc interacts both with M1 protein and M23 protein to form OAP. AQP4-Luc must associate with both the M1 and M23 protein in order to polarize. A-syntrophin is dependent on the amount of AQP4ex found in brain cells in order to reach its perivascular pole. OAPs containing the M1/M23 proteins domain are not capable to form the perivascular pole, which may explain the mislocalization AQP4–Luc.

Water homeostasis plays a key role in the CNS. AQP4 regulates volume, osmotic composition and volume within compartments. Even slight changes in volume or osmolarity within the brain can affect neuronal activity. AQP4 therefore is a target of neuromyelitis optica antibodies.

In vivo, cell culture studies show that AQP4 ligands play critical roles in cell migration and substrate adhesion. AQP4Luc is an excellent tool to study the role of AQP4 within these processes. Understanding the role of AQP4 within human tissues is crucial. This study will help us to understand its role as a regulator of water channel activity and in supramolecular order.

The extracellular loops of AQP4 influence the binding of IgG. OAPs can form three-dimensional epitopes when they are bound to syntrophin. This is characteristic of autoimmune disorders. Mutations in these loops reduce NMO-IgG bind, thereby reducing the ability for these autoantibodies interact with specific target molecules. AQP4–Luc is an effective treatment for autoimmune diseases.

AQP4 Luc constructions

Boster Bio Laboratory discovered a new way to increase AQP expression, the AQP4–Luc constructs. HuNoVVP1 promotes the Caco2 cell expression of AQP1 gene. HuNoVVP1 promotes AQP1 gene expression, but not AQP4.

HaCaT cells were transfected using 0.2 mg of promoter/expression plasmids. After 24 h, the cells could be harvested for transfection with different expression plasmids. To perform transfection experiments, agerin (20 mg/mL), was added to the cells culture medium. GAPDH expression is used as an internal check.

Transfection of AHE-Luc-pheromone-p-AChR-P-EGFP-luciferase into HaCaT keratinocytes resulted in enhanced mRNA levels of AQP3. You can also induce the gene using a reporter vector. Regardless what target you choose, the AQP4–Luc constructs in BosterBio Laboratory provide the genetic information needed to make vital biological decisions.

The AQP1 Promoter is critical for regulating AQP1's expression. HuNoV promoter activity requires VP1, a protein which promotes transcription AQP1/GAPDH. To test this hypothesis, AQP1-Luc and AQP4-Luc constructs were co-transfected in Caco2 cells, and their activity was detected by Firefly luciferase expression.

UVB radiation at 30 mJ/cm2 reduces AQP3 expression within HaCaT Keratinocytes. HaCaT cells can also be used to overcome UVB-induced suppressions of AQP3 expression. We are excited about this new approach to boosting AQP3 expression in HaCaT cell.

After lentivirus transduction using LentiHuNoV or LentiVP1 reagents, transient expression of AQP1 was demonstrated. HuNoV significantly decreased IEB TEER. Bacopaside II inhibits FITC-dextran penetration. Using the new approach, we hope to improve human health.

Constructs of the AQP7 Marker

Two NCS-related glycerol glycerol channels were used to create AQP7 Marker constructs for a Boster Bio assay. These glycerol channels comprise two monomers containing three glycerol molecules, one in each monomeric pore. The GlpF construct was also developed, but it does not achieve the expected increase in glycerol permeation.

AQP7's pore entry at EV is larger than GlpF. In both aquaglyceroporins, the four side chains contribute to constriction of the entrance. Both proteins also have three pore-lining amino acids in an inward-facing configuration. The side chains in GlpF and AQP7 adopt two distinct conformations.

AQP7's pore-forming domain contains NPS motifs and NAA motifs. These residues can be isotropic in aqueous solutions and their tilt angles are one and zero, respectively. These proteins are extremely stable, making them an excellent candidate to be used in biochemical and functional studies. Despite their differences, AQP7 is extremely stable in aqueous solutions. This stability is unaffected pH and other ionic and/or electrolyte concentrations.

AQP7 can be found in the testis and sperm. It may facilitate water expulsion during cytoplasmic, which is a process in the developing embryo. This function could be analogous to Aqy1 in yeast.

AQP1 promotes the production of a variety of proteins in the intestinal epithelial cells line. HuNoV promotes AQP1 gene expression in Caco2 cell lines. It promotes AQP7, but not AQP4.